or mitochondria. Post translational modification of KIAA0090 can occur. 54 possible sites of phosphorylation exist; 33 serines, 10 threonines, and 11 tyrosines. 3 sites of N-linked glycosylation are present at residues 370, 818, and 913 The signal peptide can be cleaved between residues 21 and 22. This information is graphically displayed in Figure 3. Structure beyond the primary remains predicative. Bioinformatic analysis yields consensus data that is also displayed in Figure 3. The protein is highly conserved throughout Eukaryotes both in multi and single cellular organisms. This includes but is not limited to animals, plants, fungi, and protists. The WD40 like domain COG1520 is KIAA0090s only identified functional effector domain. WD40 containing proteins are signal transducers involved in transduction of signals to binding factors, the centromeres, and other effectors. Coimmunoprecipitation experiments have proven KIAA0090 interaction with these types of proteins; specifically the centromeric protein CENPH, the BAX Inhibitor TMBI4, the ADP ribosylation factor ARF6, the kinase TNIK, and the transcriptional repressor T22D1. The number of splice variants indicates this list is probably not definitive. As further characterization is completed additional interactions would be expected. References Genes on human chromosome 1